ID A0A0E7UDX8_BORPT Unreviewed; 244 AA.
AC A0A0E7UDX8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=(S)-2-haloacid dehalogenase {ECO:0000256|RuleBase:RU368077};
DE EC=3.8.1.2 {ECO:0000256|RuleBase:RU368077};
DE AltName: Full=2-haloalkanoic acid dehalogenase {ECO:0000256|RuleBase:RU368077};
DE AltName: Full=Halocarboxylic acid halidohydrolase {ECO:0000256|RuleBase:RU368077};
DE AltName: Full=L-2-haloacid dehalogenase {ECO:0000256|RuleBase:RU368077};
GN Name=hdl IVa {ECO:0000313|EMBL:SUV65235.1};
GN ORFNames=NCTC10911_02277 {ECO:0000313|EMBL:SUV65235.1};
OS Bordetella pertussis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=520 {ECO:0000313|EMBL:SUV65235.1, ECO:0000313|Proteomes:UP000255014};
RN [1] {ECO:0000313|EMBL:SUV65235.1, ECO:0000313|Proteomes:UP000255014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10911 {ECO:0000313|EMBL:SUV65235.1,
RC ECO:0000313|Proteomes:UP000255014};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolytic dehalogenation of small (S)-2-
CC haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic
CC acids. {ECO:0000256|RuleBase:RU368077}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an (S)-2-haloacid + H2O = a (2R)-2-hydroxycarboxylate + a
CC halide anion + H(+); Xref=Rhea:RHEA:11192, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:58314,
CC ChEBI:CHEBI:137405; EC=3.8.1.2;
CC Evidence={ECO:0000256|RuleBase:RU368077};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. S-2-
CC haloalkanoic acid dehalogenase family. {ECO:0000256|RuleBase:RU368077}.
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DR EMBL; UFTT01000002; SUV65235.1; -; Genomic_DNA.
DR RefSeq; WP_010930696.1; NZ_UIGD01000006.1.
DR AlphaFoldDB; A0A0E7UDX8; -.
DR OMA; WHRLNPW; -.
DR Proteomes; UP000255014; Unassembled WGS sequence.
DR GO; GO:0018784; F:(S)-2-haloacid dehalogenase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.150.750; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006328; 2-HAD.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR01493; HAD-SF-IA-v2; 1.
DR NCBIfam; TIGR01428; HAD_type_II; 1.
DR PANTHER; PTHR43316:SF3; HALOACID DEHALOGENASE, TYPE II (AFU_ORTHOLOGUE AFUA_2G07750)-RELATED; 1.
DR PANTHER; PTHR43316; HYDROLASE, HALOACID DELAHOGENASE-RELATED; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU368077, ECO:0000313|EMBL:SUV65235.1}.
SQ SEQUENCE 244 AA; 26922 MW; CB1E9AB1A4BC4DA7 CRC64;
MEPVRGMDIE VLFFDVLGTV VDWRGSIADE VAAFLKRHEL PHVDAHQFAD AWVGQYDAAI
EPIRAGQRAF APLDIINMEN LQACLAQFDL APARFARSEL ETLNHAWHKL RPWPDSVAGI
AQLKQRFIVA PLSDGHTRLL VDMAKHAGLP WDMVFGADAS RSYKPAPQAY LHACALLDVP
PQRAMLVAAH GYDLDAARSC GLKTAYVQRQ RAADPSKAGY RGAPENWDYQ AGSLTELAQL
LAKA
//
